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Q9UIG0

- BAZ1B_HUMAN

UniProt

Q9UIG0 - BAZ1B_HUMAN

Protein

Tyrosine-protein kinase BAZ1B

Gene

BAZ1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (30 Aug 2002)
      Previous versions | rss
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    Functioni

    Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. In the WINAC complex, plays an essential role by targeting the complex to acetylated histones, an essential step for VDR-promoter association.6 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 Publication

    Cofactori

    Manganese.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1184 – 123451PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. chromatin binding Source: UniProtKB
    3. histone kinase activity Source: UniProtKB
    4. lysine-acetylated histone binding Source: UniProtKB
    5. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    6. protein binding Source: UniProtKB
    7. protein tyrosine kinase activity Source: UniProtKB
    8. vitamin D receptor activator activity Source: Ensembl
    9. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. chromatin assembly or disassembly Source: Ensembl
    3. chromatin-mediated maintenance of transcription Source: BHF-UCL
    4. double-strand break repair Source: BHF-UCL
    5. heart morphogenesis Source: BHF-UCL
    6. histone phosphorylation Source: UniProtKB
    7. peptidyl-tyrosine phosphorylation Source: GOC
    8. regulation of transcription, DNA-templated Source: BHF-UCL
    9. transcription, DNA-templated Source: BHF-UCL

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    DNA damage, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase BAZ1B (EC:2.7.10.2)
    Alternative name(s):
    Bromodomain adjacent to zinc finger domain protein 1B
    Williams syndrome transcription factor
    Williams-Beuren syndrome chromosomal region 10 protein
    Williams-Beuren syndrome chromosomal region 9 protein
    hWALp2
    Gene namesi
    Name:BAZ1B
    Synonyms:WBSC10, WBSCR10, WBSCR9, WSTF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:961. BAZ1B.

    Subcellular locationi

    Nucleus 2 PublicationsPROSITE-ProRule annotation
    Note: Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase via its association with PCNA.

    GO - Cellular componenti

    1. condensed chromosome Source: Ensembl
    2. nucleus Source: UniProtKB-SubCell
    3. pericentric heterochromatin Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    BAZ1B is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of BAZ1B may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi338 – 3381C → A: Loss of tyrosine-protein kinase activity. 1 Publication

    Keywords - Diseasei

    Williams-Beuren syndrome

    Organism-specific databases

    Orphaneti904. Williams syndrome.
    PharmGKBiPA25271.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14831483Tyrosine-protein kinase BAZ1BPRO_0000211170Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei161 – 1611PhosphoserineBy similarity
    Modified residuei266 – 2661Phosphothreonine1 Publication
    Modified residuei330 – 3301Phosphoserine1 Publication
    Modified residuei345 – 3451Phosphoserine1 Publication
    Modified residuei347 – 3471Phosphoserine2 Publications
    Modified residuei349 – 3491Phosphoserine2 Publications
    Modified residuei361 – 3611Phosphoserine1 Publication
    Modified residuei374 – 3741Phosphoserine1 Publication
    Modified residuei699 – 6991Phosphoserine1 Publication
    Modified residuei705 – 7051Phosphoserine3 Publications
    Modified residuei708 – 7081Phosphoserine1 Publication
    Modified residuei716 – 7161Phosphoserine1 Publication
    Modified residuei947 – 9471Phosphoserine1 Publication
    Modified residuei1315 – 13151Phosphoserine1 Publication
    Modified residuei1335 – 13351N6-acetyllysineBy similarity
    Modified residuei1342 – 13421Phosphoserine3 Publications
    Modified residuei1468 – 14681Phosphoserine5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UIG0.
    PaxDbiQ9UIG0.
    PRIDEiQ9UIG0.

    PTM databases

    PhosphoSiteiQ9UIG0.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with high levels of expression in heart, brain, placenta, skeletal muscle and ovary.

    Developmental stagei

    Expressed at equal levels in 19-23 weeks old fetal tissues.

    Gene expression databases

    BgeeiQ9UIG0.
    CleanExiHS_BAZ1B.
    GenevestigatoriQ9UIG0.

    Organism-specific databases

    HPAiCAB037081.
    CAB037158.

    Interactioni

    Subunit structurei

    Interacts with MYO1C By similarity. Interacts with CDT1. Interacts with SMARCA5/SNF2H; the interaction is direct and forms the WICH complex. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with VDR; in a ligand-dependent manner. Interacts with PCNA; the interaction is direct.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SMARCA5O602646EBI-927482,EBI-352588

    Protein-protein interaction databases

    BioGridi114497. 50 interactions.
    DIPiDIP-35642N.
    IntActiQ9UIG0. 9 interactions.
    MINTiMINT-1894324.
    STRINGi9606.ENSP00000342434.

    Structurei

    Secondary structure

    1
    1483
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni1188 – 11903
    Turni1203 – 12053
    Helixi1211 – 12144
    Turni1229 – 12313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F62NMR-A1185-1235[»]
    ProteinModelPortaliQ9UIG0.
    SMRiQ9UIG0. Positions 1185-1235, 1346-1418.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UIG0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 126107WACPROSITE-ProRule annotationAdd
    BLAST
    Domaini604 – 66865DDTPROSITE-ProRule annotationAdd
    BLAST
    Domaini1356 – 142671BromoPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 345345Mediates the tyrosine-protein kinase activityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili533 – 58654Sequence AnalysisAdd
    BLAST
    Coiled coili768 – 81447Sequence AnalysisAdd
    BLAST
    Coiled coili850 – 89344Sequence AnalysisAdd
    BLAST
    Coiled coili1245 – 128339Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi207 – 2137C motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi306 – 578273Lys-richAdd
    BLAST
    Compositional biasi1261 – 127313Poly-GluAdd
    BLAST

    Domaini

    The N-terminal part (1-345), including the WAC domain and the C motif, mediates the tyrosine-protein kinase activity.1 Publication
    The bromo domain mediates the specific interaction with acetylated histones.1 Publication

    Sequence similaritiesi

    Belongs to the WAL family. BAZ1B subfamily.Curated
    Contains 1 bromo domain.PROSITE-ProRule annotation
    Contains 1 DDT domain.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
    Contains 1 WAC domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1184 – 123451PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5076.
    HOVERGENiHBG050668.
    InParanoidiQ9UIG0.
    KOiK11658.
    OMAiDEDYCPR.
    OrthoDBiEOG72G17K.
    PhylomeDBiQ9UIG0.
    TreeFamiTF106397.

    Family and domain databases

    Gene3Di1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR018500. DDT_dom_subgr.
    IPR018501. DDT_dom_superfamily.
    IPR028942. WHIM1_dom.
    IPR028941. WHIM2_dom.
    IPR028935. WHIM3_domain.
    IPR013136. WSTF_Acf1_Cbp146.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00439. Bromodomain. 1 hit.
    PF00628. PHD. 1 hit.
    PF10537. WAC_Acf1_DNA_bd. 1 hit.
    PF15612. WHIM1. 1 hit.
    PF15613. WHIM2. 1 hit.
    PF15614. WHIM3. 1 hit.
    [Graphical view]
    PRINTSiPR00503. BROMODOMAIN.
    SMARTiSM00297. BROMO. 1 hit.
    SM00571. DDT. 1 hit.
    SM00249. PHD. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
    PS50014. BROMODOMAIN_2. 1 hit.
    PS50827. DDT. 1 hit.
    PS51136. WAC. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UIG0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW     50
    TCKSTGSSQL THKEAWEEEQ EVAELLKEEF PAWYEKLVLE MVHHNTASLE 100
    KLVDTAWLEI MTKYAVGEEC DFEVGKEKML KVKIVKIHPL EKVDEEATEK 150
    KSDGACDSPS SDKENSSQIA QDHQKKETVV KEDEGRRESI NDRARRSPRK 200
    LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS LIRTERPPNK 250
    EIVRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT 300
    LNPSTKRKNT GSPDRKPSKK SKTDNSSLSS PLNPKLWCHV HLKKSLSGSP 350
    LKVKNSKNSK SPEEHLEEMM KMMSPNKLHT NFHIPKKGPP AKKPGKHSDK 400
    PLKAKGRSKG ILNGQKSTGN SKSPKKGLKT PKTKMKQMTL LDMAKGTQKM 450
    TRAPRNSGGT PRTSSKPHKH LPPAALHLIA YYKENKDRED KRSALSCVIS 500
    KTARLLSSED RARLPEELRS LVQKRYELLE HKKRWASMSE EQRKEYLKKK 550
    REELKKKLKE KAKERREKEM LERLEKQKRY EDQELTGKNL PAFRLVDTPE 600
    GLPNTLFGDV AMVVEFLSCY SGLLLPDAQY PITAVSLMEA LSADKGGFLY 650
    LNRVLVILLQ TLLQDEIAED YGELGMKLSE IPLTLHSVSE LVRLCLRRSD 700
    VQEESEGSDT DDNKDSAAFE DNEVQDEFLE KLETSEFFEL TSEEKLQILT 750
    ALCHRILMTY SVQDHMETRQ QMSAELWKER LAVLKEENDK KRAEKQKRKE 800
    MEAKNKENGK VENGLGKTDR KKEIVKFEPQ VDTEAEDMIS AVKSRRLLAI 850
    QAKKEREIQE REMKVKLERQ AEEERIRKHK AAAEKAFQEG IAKAKLVMRR 900
    TPIGTDRNHN RYWLFSDEVP GLFIEKGWVH DSIDYRFNHH CKDHTVSGDE 950
    DYCPRSKKAN LGKNASMNTQ HGTATEVAVE TTTPKQGQNL WFLCDSQKEL 1000
    DELLNCLHPQ GIRESQLKER LEKRYQDIIH SIHLARKPNL GLKSCDGNQE 1050
    LLNFLRSDLI EVATRLQKGG LGYVEETSEF EARVISLEKL KDFGECVIAL 1100
    QASVIKKFLQ GFMAPKQKRR KLQSEDSAKT EEVDEEKKMV EEAKVASALE 1150
    KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI 1200
    LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPATARRNS RGRNYTEESA 1250
    SEDSEDDESD EEEEEEEEEE EEEDYEVAGL RLRPRKTIRG KHSVIPPAAR 1300
    SGRRPGKKPH STRRSQPKAP PVDDAEVDEL VLQTKRSSRR QSLELQKCEE 1350
    ILHKIVKYRF SWPFREPVTR DEAEDYYDVI THPMDFQTVQ NKCSCGSYRS 1400
    VQEFLTDMKQ VFTNAEVYNC RGSHVLSCMV KTEQCLVALL HKHLPGHPYV 1450
    RRKRKKFPDR LAEDEGDSEP EAVGQSRGRR QKK 1483
    Length:1,483
    Mass (Da):170,903
    Last modified:August 30, 2002 - v2
    Checksum:i0CC146FEBB954261
    GO
    Isoform 2 (identifier: Q9UIG0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         660-663: Missing.

    Show »
    Length:1,479
    Mass (Da):170,447
    Checksum:iD0F1A5559EB52F78
    GO

    Sequence cautioni

    The sequence AAH65029.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAC97879.1 differs from that shown. Reason: Frameshift at positions 1031, 1042 and 1422.
    The sequence BAA89210.1 differs from that shown. Reason: Frameshift at position 1478.
    The sequence AAD04720.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141K → N in BAA89210. (PubMed:10662543)Curated
    Sequence conflicti22 – 221L → F in BAA89210. (PubMed:10662543)Curated
    Sequence conflicti136 – 1361K → E in AAD08675. (PubMed:9858827)Curated
    Sequence conflicti823 – 8231E → R in BAA89210. (PubMed:10662543)Curated
    Sequence conflicti1191 – 11911R → P in BAA89210. (PubMed:10662543)Curated
    Sequence conflicti1354 – 13541K → M in AAC97879. (PubMed:9828126)Curated
    Sequence conflicti1438 – 14381A → V in BAA89210. (PubMed:10662543)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei660 – 6634Missing in isoform 2. 1 PublicationVSP_000552

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF084479 mRNA. Translation: AAD08675.1.
    AF072810 mRNA. Translation: AAC97879.1. Frameshift.
    AB032253 mRNA. Translation: BAA89210.1. Frameshift.
    AC005074 Genomic DNA. Translation: AAD04720.1. Sequence problems.
    AC005089 Genomic DNA. Translation: AAP22332.1.
    CH471200 Genomic DNA. Translation: EAW69680.1.
    CH471200 Genomic DNA. Translation: EAW69681.1.
    BC065029 mRNA. Translation: AAH65029.1. Sequence problems.
    BC136520 mRNA. Translation: AAI36521.1.
    CCDSiCCDS5549.1. [Q9UIG0-1]
    RefSeqiNP_115784.1. NM_032408.3. [Q9UIG0-1]
    UniGeneiHs.743372.

    Genome annotation databases

    EnsembliENST00000339594; ENSP00000342434; ENSG00000009954. [Q9UIG0-1]
    ENST00000404251; ENSP00000385442; ENSG00000009954. [Q9UIG0-1]
    GeneIDi9031.
    KEGGihsa:9031.
    UCSCiuc003tyc.3. human. [Q9UIG0-1]

    Polymorphism databases

    DMDMi22653670.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF084479 mRNA. Translation: AAD08675.1 .
    AF072810 mRNA. Translation: AAC97879.1 . Frameshift.
    AB032253 mRNA. Translation: BAA89210.1 . Frameshift.
    AC005074 Genomic DNA. Translation: AAD04720.1 . Sequence problems.
    AC005089 Genomic DNA. Translation: AAP22332.1 .
    CH471200 Genomic DNA. Translation: EAW69680.1 .
    CH471200 Genomic DNA. Translation: EAW69681.1 .
    BC065029 mRNA. Translation: AAH65029.1 . Sequence problems.
    BC136520 mRNA. Translation: AAI36521.1 .
    CCDSi CCDS5549.1. [Q9UIG0-1 ]
    RefSeqi NP_115784.1. NM_032408.3. [Q9UIG0-1 ]
    UniGenei Hs.743372.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F62 NMR - A 1185-1235 [» ]
    ProteinModelPortali Q9UIG0.
    SMRi Q9UIG0. Positions 1185-1235, 1346-1418.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114497. 50 interactions.
    DIPi DIP-35642N.
    IntActi Q9UIG0. 9 interactions.
    MINTi MINT-1894324.
    STRINGi 9606.ENSP00000342434.

    PTM databases

    PhosphoSitei Q9UIG0.

    Polymorphism databases

    DMDMi 22653670.

    Proteomic databases

    MaxQBi Q9UIG0.
    PaxDbi Q9UIG0.
    PRIDEi Q9UIG0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000339594 ; ENSP00000342434 ; ENSG00000009954 . [Q9UIG0-1 ]
    ENST00000404251 ; ENSP00000385442 ; ENSG00000009954 . [Q9UIG0-1 ]
    GeneIDi 9031.
    KEGGi hsa:9031.
    UCSCi uc003tyc.3. human. [Q9UIG0-1 ]

    Organism-specific databases

    CTDi 9031.
    GeneCardsi GC07M072854.
    HGNCi HGNC:961. BAZ1B.
    HPAi CAB037081.
    CAB037158.
    MIMi 605681. gene.
    neXtProti NX_Q9UIG0.
    Orphaneti 904. Williams syndrome.
    PharmGKBi PA25271.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOVERGENi HBG050668.
    InParanoidi Q9UIG0.
    KOi K11658.
    OMAi DEDYCPR.
    OrthoDBi EOG72G17K.
    PhylomeDBi Q9UIG0.
    TreeFami TF106397.

    Miscellaneous databases

    ChiTaRSi BAZ1B. human.
    EvolutionaryTracei Q9UIG0.
    GeneWikii BAZ1B.
    GenomeRNAii 9031.
    NextBioi 33835.
    PROi Q9UIG0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UIG0.
    CleanExi HS_BAZ1B.
    Genevestigatori Q9UIG0.

    Family and domain databases

    Gene3Di 1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR018500. DDT_dom_subgr.
    IPR018501. DDT_dom_superfamily.
    IPR028942. WHIM1_dom.
    IPR028941. WHIM2_dom.
    IPR028935. WHIM3_domain.
    IPR013136. WSTF_Acf1_Cbp146.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00439. Bromodomain. 1 hit.
    PF00628. PHD. 1 hit.
    PF10537. WAC_Acf1_DNA_bd. 1 hit.
    PF15612. WHIM1. 1 hit.
    PF15613. WHIM2. 1 hit.
    PF15614. WHIM3. 1 hit.
    [Graphical view ]
    PRINTSi PR00503. BROMODOMAIN.
    SMARTi SM00297. BROMO. 1 hit.
    SM00571. DDT. 1 hit.
    SM00249. PHD. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
    PS50014. BROMODOMAIN_2. 1 hit.
    PS50827. DDT. 1 hit.
    PS51136. WAC. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of the WBSCR9 gene, encoding a novel transcriptional regulator, in the Williams-Beuren syndrome deletion at 7q11.23."
      Peoples R.J., Cisco M.J., Kaplan P., Francke U.
      Cytogenet. Cell Genet. 82:238-246(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "A novel human gene, WSTF, is deleted in Williams Syndrome."
      Lu X., Meng X., Morris C.A., Keating M.T.
      Genomics 54:241-249(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN WBS.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Testis.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    7. "WSTF-ISWI chromatin remodeling complex targets heterochromatic replication foci."
      Bozhenok L., Wade P.A., Varga-Weisz P.
      EMBO J. 21:2231-2241(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
      Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
      Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
    9. "The Williams syndrome transcription factor interacts with PCNA to target chromatin remodelling by ISWI to replication foci."
      Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S., Ferreira F., Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D.
      Nat. Cell Biol. 6:1236-1244(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PCNA.
    10. "Ligand-induced transrepression by VDR through association of WSTF with acetylated histones."
      Fujiki R., Kim M.-S., Sasaki Y., Yoshimura K., Kitagawa H., Kato S.
      EMBO J. 24:3881-3894(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VDR, DOMAIN BROMO.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1342 AND SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription."
      Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.
      J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE B-WICH COMPLEX.
    13. "Identification of novel human Cdt1-binding proteins by a proteomics approach: proteolytic regulation by APC/CCdh1."
      Sugimoto N., Kitabayashi I., Osano S., Tatsumi Y., Yugawa T., Narisawa-Saito M., Matsukage A., Kiyono T., Fujita M.
      Mol. Biol. Cell 19:1007-1021(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CDT1.
    14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-374; SER-699; SER-705; SER-708; SER-716; SER-947; SER-1315 AND SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF CYS-338.
    18. "Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions."
      Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.
      Nature 458:591-596(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-705, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266; SER-345; SER-347; SER-349; SER-361; SER-1342 AND SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-349; SER-705; SER-1342 AND SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor."
      Pascual J., Martinez-Yamout M., Dyson H.J., Wright P.E.
      J. Mol. Biol. 304:723-729(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1185-1235.

    Entry informationi

    Entry nameiBAZ1B_HUMAN
    AccessioniPrimary (citable) accession number: Q9UIG0
    Secondary accession number(s): B9EGK3
    , D3DXE9, O95039, O95247, O95277, Q6P1K4, Q86UJ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2002
    Last sequence update: August 30, 2002
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3